ID TRI23_HUMAN Reviewed; 574 AA. AC P36406; Q9BZY4; Q9BZY5; DT 01-JUN-1994, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1994, sequence version 1. DT 02-SEP-2026, entry version 226. DE RecName: Full=E3 ubiquitin-protein ligase TRIM23; DE EC=2.3.2.27 {ECO:0000269|PubMed:38769438}; DE AltName: Full=ADP-ribosylation factor domain-containing protein 1; DE AltName: Full=GTP-binding protein ARD-1; DE AltName: Full=RING finger protein 46; DE AltName: Full=RING-type E3 ubiquitin transferase TRIM23 {ECO:0000305}; DE AltName: Full=Tripartite motif-containing protein 23; GN Name=TRIM23; Synonyms=ARD1, ARFD1, RNF46; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM ALPHA). RX PubMed=8473324; DOI=10.1016/s0021-9258(18)52945-8; RA Mishima K., Tsuchiya M., Nightingale M.S., Moss J., Vaughan M.; RT "ARD 1, a 64-kDa guanine nucleotide-binding protein with a carboxyl- RT terminal ADP-ribosylation factor domain."; RL J. Biol. Chem. 268:8801-8807(1993). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS ALPHA; BETA AND GAMMA). RX PubMed=11331580; DOI=10.1093/emboj/20.9.2140; RA Reymond A., Meroni G., Fantozzi A., Merla G., Cairo S., Luzi L., RA Riganelli D., Zanaria E., Messali S., Cainarca S., Guffanti A., Minucci S., RA Pelicci P.G., Ballabio A.; RT "The tripartite motif family identifies cell compartments."; RL EMBO J. 20:2140-2151(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM ALPHA). RC TISSUE=Brain; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [4] RP SUBCELLULAR LOCATION. RX PubMed=9671726; DOI=10.1073/pnas.95.15.8613; RA Vitale N., Horiba K., Ferrans V.J., Moss J., Vaughan M.; RT "Localization of ADP-ribosylation factor domain protein 1 (ARD1) in RT lysosomes and Golgi apparatus."; RL Proc. Natl. Acad. Sci. U.S.A. 95:8613-8618(1998). RN [5] RP INTERACTION WITH PSCD1, AND MUTAGENESIS OF THR-418 AND LYS-458. RX PubMed=10748148; DOI=10.1074/jbc.m909642199; RA Vitale N., Pacheco-Rodriguez G., Ferrans V.J., Riemenschneider W., Moss J., RA Vaughan M.; RT "Specific functional interaction of human cytohesin-1 and ADP-ribosylation RT factor domain protein (ARD1)."; RL J. Biol. Chem. 275:21331-21339(2000). RN [6] RP FUNCTION, AND MUTAGENESIS OF CYS-34 AND HIS-53. RX PubMed=15684077; DOI=10.1073/pnas.0409800102; RA Vichi A., Payne D.M., Pacheco-Rodriguez G., Moss J., Vaughan M.; RT "E3 ubiquitin ligase activity of the trifunctional ARD1 (ADP-ribosylation RT factor domain protein 1)."; RL Proc. Natl. Acad. Sci. U.S.A. 102:1945-1950(2005). RN [7] RP INTERACTION WITH HUMAN CYTOMEGALOVIRUS PROTEIN UL144. RX PubMed=19176615; DOI=10.1128/jvi.02072-08; RA Poole E., Groves I., MacDonald A., Pang Y., Alcami A., Sinclair J.; RT "Identification of TRIM23 as a cofactor involved in the regulation of NF- RT kappaB by human cytomegalovirus."; RL J. Virol. 83:3581-3590(2009). RN [8] RP FUNCTION, INTERACTION WITH TBK1 AND SQSTM1, AND SUBCELLULAR LOCATION. RX PubMed=28871090; DOI=10.1038/s41564-017-0017-2; RA Sparrer K.M.J., Gableske S., Zurenski M.A., Parker Z.M., Full F., RA Baumgart G.J., Kato J., Pacheco-Rodriguez G., Liang C., Pornillos O., RA Moss J., Vaughan M., Gack M.U.; RT "TRIM23 mediates virus-induced autophagy via activation of TBK1."; RL Nat. Microbiol. 2:1543-1557(2017). RN [9] RP FUNCTION, AND INTERACTION WITH HERPES VIRUS 1/HHV-1 PROTEIN US11 (MICROBIAL RP INFECTION). RX PubMed=31189704; DOI=10.1128/jvi.00497-19; RA Liu X., Matrenec R., Gack M.U., He B.; RT "Disassembly of the TRIM23-TBK1 Complex by the Us11 Protein of Herpes RT Simplex Virus 1 Impairs Autophagy."; RL J. Virol. 93:0-0(2019). RN [10] RP FUNCTION, SUBCELLULAR LOCATION, AND CATALYTIC ACTIVITY. RX PubMed=38769438; DOI=10.1038/s44318-024-00120-6; RA Zhan W., Li Z., Zhang J., Liu Y., Liu G., Li B., Shen R., Jiang Y., RA Shang W., Gao S., Wu H., Wang Y., Chen W., Wang Z.; RT "Energy stress promotes P-bodies formation via lysine-63-linked RT polyubiquitination of HAX1."; RL EMBO J. 43:2759-2788(2024). RN [11] RP FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-39, UBIQUITINATION, RP AND MUTAGENESIS OF SER-39. RX PubMed=40360474; DOI=10.1038/s41467-025-59338-5; RA Acharya D., Sayyad Z., Hoenigsperger H., Hirschenberger M., Zurenski M., RA Balakrishnan K., Zhu J., Gableske S., Kato J., Zhang S.Y., Casanova J.L., RA Moss J., Sparrer K.M.J., Gack M.U.; RT "TRIM23 mediates cGAS-induced autophagy in anti-HSV defense."; RL Nat. Commun. 16:4418-4418(2025). RN [12] RP X-RAY CRYSTALLOGRAPHY (1.81 ANGSTROMS) OF 1-123, SUBUNIT, INTERACTION WITH RP UBE2D2, AND DOMAIN. RX PubMed=28681414; DOI=10.1002/prot.25348; RA Dawidziak D.M., Sanchez J.G., Wagner J.M., Ganser-Pornillos B.K., RA Pornillos O.; RT "Structure and catalytic activation of the TRIM23 RING E3 ubiquitin RT ligase."; RL Proteins 85:1957-1961(2017). CC -!- FUNCTION: E3 ubiquitin ligase that harbors GTPase activity encoded by CC the C-terminal ARF domain. Plays an essential role in autophagy CC activation during viral infection (PubMed:31189704, PubMed:40360474). CC Mechanistically, activates TANK-binding kinase 1/TBK1 by facilitating CC its dimerization and ability to phosphorylate the selective autophagy CC receptor SQSTM1 (PubMed:28871090, PubMed:31189704). In order to achieve CC this function, TRIM23 mediates 'Lys-27'-linked auto-ubiquitination of CC its ADP-ribosylation factor (ARF) domain to induce its GTPase activity CC and its recruitment to autophagosomes (PubMed:28871090). Catalyzes CC 'Lys-63'-linked polyubiquitination of HAX1 that triggers its liquid- CC liquid phase separation (LLPS) and contributes to P-bodies assembly CC induced by energy stress (PubMed:38769438). CC {ECO:0000269|PubMed:15684077, ECO:0000269|PubMed:28871090, CC ECO:0000269|PubMed:31189704, ECO:0000269|PubMed:38769438, CC ECO:0000269|PubMed:40360474}. CC -!- FUNCTION: (Microbial infection) Mediates TRAF6 auto-ubiquitination in CC the presence of human cytomegalovirus protein UL144, resulting in the CC virally controlled activation of NF-kappa-B stimulation at early times CC of HCMV infection. {ECO:0000269|PubMed:15684077}. CC -!- CATALYTIC ACTIVITY: CC Reaction=S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + CC [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L- CC cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine.; CC EC=2.3.2.27; Evidence={ECO:0000269|PubMed:38769438}; CC -!- PATHWAY: Protein modification; protein ubiquitination. CC {ECO:0000269|PubMed:38769438}. CC -!- SUBUNIT: Homodimer. Interacts with PSCD1. Interacts with UBE2D2 CC (PubMed:28681414). Interacts with TBK1 (via N-terminal kinase domain) CC and p62/SQSTM1. {ECO:0000269|PubMed:10748148, CC ECO:0000269|PubMed:28681414, ECO:0000269|PubMed:28871090}. CC -!- SUBUNIT: (Microbial infection) Interacts with human cytomegalovirus CC protein UL144; this interaction might cause autoubiquitination of CC TRAF6, leading to NF-kappa-B activation. {ECO:0000269|PubMed:19176615}. CC -!- SUBUNIT: (Microbial infection) Interacts with human herpes virus 1 CC protein US11; this interaction disrupts the TRIM23-TBK1 complex, which CC subsequently suppresses autophagy and autophagy-mediated virus CC restriction. {ECO:0000269|PubMed:31189704}. CC -!- INTERACTION: CC P36406; A0A0S2Z3G1: ACTN4; NbExp=3; IntAct=EBI-740098, EBI-16430749; CC P36406; Q96IX9: ANKRD36BP1; NbExp=3; IntAct=EBI-740098, EBI-744859; CC P36406; Q3KP44: ANKRD55; NbExp=3; IntAct=EBI-740098, EBI-14493093; CC P36406; Q9Y2T2: AP3M1; NbExp=3; IntAct=EBI-740098, EBI-2371151; CC P36406; P29972: AQP1; NbExp=6; IntAct=EBI-740098, EBI-745213; CC P36406; Q8N6T3: ARFGAP1; NbExp=3; IntAct=EBI-740098, EBI-716933; CC P36406; Q9NR81: ARHGEF3; NbExp=5; IntAct=EBI-740098, EBI-10312733; CC P36406; Q8N5M1: ATPAF2; NbExp=7; IntAct=EBI-740098, EBI-1166928; CC P36406; P54253: ATXN1; NbExp=6; IntAct=EBI-740098, EBI-930964; CC P36406; Q99933: BAG1; NbExp=5; IntAct=EBI-740098, EBI-1030678; CC P36406; Q6AI39: BICRAL; NbExp=3; IntAct=EBI-740098, EBI-1012434; CC P36406; Q0VDD7: BRME1; NbExp=4; IntAct=EBI-740098, EBI-741210; CC P36406; Q53TS8: C2CD6; NbExp=3; IntAct=EBI-740098, EBI-739879; CC P36406; Q9H7E9: C8orf33; NbExp=3; IntAct=EBI-740098, EBI-715389; CC P36406; Q9H257: CARD9; NbExp=4; IntAct=EBI-740098, EBI-751319; CC P36406; P55212: CASP6; NbExp=3; IntAct=EBI-740098, EBI-718729; CC P36406; Q9HC52: CBX8; NbExp=3; IntAct=EBI-740098, EBI-712912; CC P36406; Q8IYE1: CCDC13; NbExp=3; IntAct=EBI-740098, EBI-10961312; CC P36406; Q8IYE0-2: CCDC146; NbExp=3; IntAct=EBI-740098, EBI-10247802; CC P36406; Q86WR0: CCDC25; NbExp=3; IntAct=EBI-740098, EBI-2690264; CC P36406; Q86Y33: CDC20B; NbExp=3; IntAct=EBI-740098, EBI-10260504; CC P36406; Q6P1J9: CDC73; NbExp=3; IntAct=EBI-740098, EBI-930143; CC P36406; Q01850: CDR2; NbExp=6; IntAct=EBI-740098, EBI-1181367; CC P36406; Q96M91: CFAP53; NbExp=3; IntAct=EBI-740098, EBI-742422; CC P36406; O43247-2: CIMIP4; NbExp=3; IntAct=EBI-740098, EBI-12093053; CC P36406; P10606: COX5B; NbExp=5; IntAct=EBI-740098, EBI-1053725; CC P36406; Q9UBL6-2: CPNE7; NbExp=3; IntAct=EBI-740098, EBI-12012272; CC P36406; Q02930-3: CREB5; NbExp=3; IntAct=EBI-740098, EBI-10192698; CC P36406; Q16527: CSRP2; NbExp=3; IntAct=EBI-740098, EBI-2959737; CC P36406; Q2TBE0: CWF19L2; NbExp=3; IntAct=EBI-740098, EBI-5453285; CC P36406; O95715: CXCL14; NbExp=3; IntAct=EBI-740098, EBI-2798068; CC P36406; O43602: DCX; NbExp=3; IntAct=EBI-740098, EBI-8646694; CC P36406; Q14565: DMC1; NbExp=3; IntAct=EBI-740098, EBI-930865; CC P36406; Q9NQL9: DMRT3; NbExp=3; IntAct=EBI-740098, EBI-9679045; CC P36406; Q92608: DOCK2; NbExp=3; IntAct=EBI-740098, EBI-448771; CC P36406; Q96CJ1: EAF2; NbExp=3; IntAct=EBI-740098, EBI-1245604; CC P36406; Q08426: EHHADH; NbExp=3; IntAct=EBI-740098, EBI-2339219; CC P36406; O15371: EIF3D; NbExp=3; IntAct=EBI-740098, EBI-353818; CC P36406; Q9H0I2: ENKD1; NbExp=3; IntAct=EBI-740098, EBI-744099; CC P36406; O95208-2: EPN2; NbExp=3; IntAct=EBI-740098, EBI-12135243; CC P36406; Q8N2X6: EXOC3-AS1; NbExp=3; IntAct=EBI-740098, EBI-749333; CC P36406; Q9BQ89: FAM110A; NbExp=6; IntAct=EBI-740098, EBI-1752811; CC P36406; Q8N9E0: FAM133A; NbExp=6; IntAct=EBI-740098, EBI-10268158; CC P36406; Q96PV7-2: FAM193B; NbExp=3; IntAct=EBI-740098, EBI-10292648; CC P36406; Q86UY5: FAM83A; NbExp=3; IntAct=EBI-740098, EBI-1384254; CC P36406; Q86YD7: FAM90A1; NbExp=6; IntAct=EBI-740098, EBI-6658203; CC P36406; Q8TES7-6: FBF1; NbExp=3; IntAct=EBI-740098, EBI-10244131; CC P36406; P22607: FGFR3; NbExp=3; IntAct=EBI-740098, EBI-348399; CC P36406; Q8NFF5-2: FLAD1; NbExp=3; IntAct=EBI-740098, EBI-11526128; CC P36406; C0H5X2: FLJ38668; NbExp=3; IntAct=EBI-740098, EBI-10176227; CC P36406; A0A0S2Z4D9: GAD1; NbExp=3; IntAct=EBI-740098, EBI-16430771; CC P36406; P23769: GATA2; NbExp=4; IntAct=EBI-740098, EBI-2806671; CC P36406; P55040: GEM; NbExp=7; IntAct=EBI-740098, EBI-744104; CC P36406; Q9NZ52-2: GGA3; NbExp=3; IntAct=EBI-740098, EBI-12075758; CC P36406; Q8NEA9: GMCL2; NbExp=3; IntAct=EBI-740098, EBI-745707; CC P36406; O95872: GPANK1; NbExp=7; IntAct=EBI-740098, EBI-751540; CC P36406; Q92917: GPKOW; NbExp=4; IntAct=EBI-740098, EBI-746309; CC P36406; Q14957: GRIN2C; NbExp=3; IntAct=EBI-740098, EBI-8285963; CC P36406; P06396: GSN; NbExp=3; IntAct=EBI-740098, EBI-351506; CC P36406; Q9GZV7: HAPLN2; NbExp=3; IntAct=EBI-740098, EBI-11956675; CC P36406; Q96CS2: HAUS1; NbExp=3; IntAct=EBI-740098, EBI-2514791; CC P36406; O14964: HGS; NbExp=3; IntAct=EBI-740098, EBI-740220; CC P36406; O00291: HIP1; NbExp=3; IntAct=EBI-740098, EBI-473886; CC P36406; P09067: HOXB5; NbExp=6; IntAct=EBI-740098, EBI-3893317; CC P36406; P01112: HRAS; NbExp=3; IntAct=EBI-740098, EBI-350145; CC P36406; P04792: HSPB1; NbExp=3; IntAct=EBI-740098, EBI-352682; CC P36406; Q9UBY9: HSPB7; NbExp=3; IntAct=EBI-740098, EBI-739361; CC P36406; Q14005-2: IL16; NbExp=3; IntAct=EBI-740098, EBI-17178971; CC P36406; Q8NA54: IQUB; NbExp=7; IntAct=EBI-740098, EBI-10220600; CC P36406; Q15040: JOSD1; NbExp=3; IntAct=EBI-740098, EBI-2510602; CC P36406; O75564-2: JRK; NbExp=3; IntAct=EBI-740098, EBI-17181882; CC P36406; Q92993: KAT5; NbExp=3; IntAct=EBI-740098, EBI-399080; CC P36406; O60333-2: KIF1B; NbExp=3; IntAct=EBI-740098, EBI-10975473; CC P36406; Q9BVG8: KIFC3; NbExp=3; IntAct=EBI-740098, EBI-2125614; CC P36406; Q9P2K6: KLHL42; NbExp=6; IntAct=EBI-740098, EBI-739890; CC P36406; P02538: KRT6A; NbExp=8; IntAct=EBI-740098, EBI-702198; CC P36406; O95678: KRT75; NbExp=3; IntAct=EBI-740098, EBI-2949715; CC P36406; Q01546: KRT76; NbExp=3; IntAct=EBI-740098, EBI-2952745; CC P36406; Q14657: LAGE3; NbExp=3; IntAct=EBI-740098, EBI-1052105; CC P36406; P13473-2: LAMP2; NbExp=3; IntAct=EBI-740098, EBI-21591415; CC P36406; Q96BZ8: LENG1; NbExp=3; IntAct=EBI-740098, EBI-726510; CC P36406; Q8TCE9: LGALS14; NbExp=3; IntAct=EBI-740098, EBI-10274069; CC P36406; O00214: LGALS8; NbExp=4; IntAct=EBI-740098, EBI-740058; CC P36406; Q96FQ7: LINC00526; NbExp=3; IntAct=EBI-740098, EBI-10286106; CC P36406; P25791: LMO2; NbExp=3; IntAct=EBI-740098, EBI-739696; CC P36406; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-740098, EBI-11742507; CC P36406; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-740098, EBI-739832; CC P36406; Q8NDC4: MORN4; NbExp=6; IntAct=EBI-740098, EBI-10269566; CC P36406; Q9BYD3: MRPL4; NbExp=3; IntAct=EBI-740098, EBI-721368; CC P36406; Q9BRJ2: MRPL45; NbExp=3; IntAct=EBI-740098, EBI-2514313; CC P36406; Q8IXL7-2: MSRB3; NbExp=3; IntAct=EBI-740098, EBI-10699187; CC P36406; Q6P444: MTFR2; NbExp=3; IntAct=EBI-740098, EBI-10252703; CC P36406; Q9P2K5-2: MYEF2; NbExp=3; IntAct=EBI-740098, EBI-10318831; CC P36406; P52179-2: MYOM1; NbExp=3; IntAct=EBI-740098, EBI-12010196; CC P36406; Q9NP98: MYOZ1; NbExp=3; IntAct=EBI-740098, EBI-744402; CC P36406; Q15742: NAB2; NbExp=3; IntAct=EBI-740098, EBI-8641936; CC P36406; Q14511-2: NEDD9; NbExp=3; IntAct=EBI-740098, EBI-11746523; CC P36406; Q9HC98: NEK6; NbExp=4; IntAct=EBI-740098, EBI-740364; CC P36406; Q9UMS0: NFU1; NbExp=3; IntAct=EBI-740098, EBI-725252; CC P36406; Q86UR1-2: NOXA1; NbExp=3; IntAct=EBI-740098, EBI-12025760; CC P36406; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-740098, EBI-741158; CC P36406; O43809: NUDT21; NbExp=3; IntAct=EBI-740098, EBI-355720; CC P36406; Q9NPJ8: NXT2; NbExp=3; IntAct=EBI-740098, EBI-752122; CC P36406; O43189: PHF1; NbExp=4; IntAct=EBI-740098, EBI-530034; CC P36406; O75928: PIAS2; NbExp=3; IntAct=EBI-740098, EBI-348555; CC P36406; O00459: PIK3R2; NbExp=3; IntAct=EBI-740098, EBI-346930; CC P36406; P78337: PITX1; NbExp=4; IntAct=EBI-740098, EBI-748265; CC P36406; Q99569: PKP4; NbExp=3; IntAct=EBI-740098, EBI-726447; CC P36406; Q9HB19: PLEKHA2; NbExp=3; IntAct=EBI-740098, EBI-4401947; CC P36406; Q9UGP5-2: POLL; NbExp=3; IntAct=EBI-740098, EBI-10320765; CC P36406; Q96HA1-2: POM121; NbExp=3; IntAct=EBI-740098, EBI-11956563; CC P36406; Q13356: PPIL2; NbExp=3; IntAct=EBI-740098, EBI-7705988; CC P36406; Q5SWA1: PPP1R15B; NbExp=3; IntAct=EBI-740098, EBI-2815482; CC P36406; Q6NYC8: PPP1R18; NbExp=3; IntAct=EBI-740098, EBI-2557469; CC P36406; Q99633: PRPF18; NbExp=3; IntAct=EBI-740098, EBI-2798416; CC P36406; Q8WWY3: PRPF31; NbExp=3; IntAct=EBI-740098, EBI-1567797; CC P36406; P25786: PSMA1; NbExp=5; IntAct=EBI-740098, EBI-359352; CC P36406; P20618: PSMB1; NbExp=3; IntAct=EBI-740098, EBI-372273; CC P36406; Q9BTL3: RAMAC; NbExp=6; IntAct=EBI-740098, EBI-744023; CC P36406; P62826: RAN; NbExp=3; IntAct=EBI-740098, EBI-286642; CC P36406; Q9UKA8: RCAN3; NbExp=3; IntAct=EBI-740098, EBI-9091952; CC P36406; Q8N443: RIBC1; NbExp=3; IntAct=EBI-740098, EBI-10265323; CC P36406; Q13671: RIN1; NbExp=3; IntAct=EBI-740098, EBI-366017; CC P36406; Q63HN8-6: RNF213; NbExp=3; IntAct=EBI-740098, EBI-10248548; CC P36406; A0A0S2Z4G9: RNF6; NbExp=3; IntAct=EBI-740098, EBI-16428950; CC P36406; Q7L4I2-2: RSRC2; NbExp=3; IntAct=EBI-740098, EBI-10256202; CC P36406; Q14D33: RTP5; NbExp=3; IntAct=EBI-740098, EBI-10217913; CC P36406; Q96T51-2: RUFY1; NbExp=3; IntAct=EBI-740098, EBI-12192715; CC P36406; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-740098, EBI-748391; CC P36406; Q9H788: SH2D4A; NbExp=3; IntAct=EBI-740098, EBI-747035; CC P36406; Q9H788-2: SH2D4A; NbExp=3; IntAct=EBI-740098, EBI-10308083; CC P36406; Q8IUQ4: SIAH1; NbExp=3; IntAct=EBI-740098, EBI-747107; CC P36406; P12236: SLC25A6; NbExp=3; IntAct=EBI-740098, EBI-356254; CC P36406; Q9H0W8: SMG9; NbExp=6; IntAct=EBI-740098, EBI-2872322; CC P36406; O95863: SNAI1; NbExp=7; IntAct=EBI-740098, EBI-1045459; CC P36406; O43623: SNAI2; NbExp=3; IntAct=EBI-740098, EBI-9876238; CC P36406; P14678-2: SNRPB; NbExp=3; IntAct=EBI-740098, EBI-372475; CC P36406; P08579: SNRPB2; NbExp=3; IntAct=EBI-740098, EBI-1053651; CC P36406; Q13573: SNW1; NbExp=3; IntAct=EBI-740098, EBI-632715; CC P36406; O60504: SORBS3; NbExp=6; IntAct=EBI-740098, EBI-741237; CC P36406; Q9NZD8: SPG21; NbExp=3; IntAct=EBI-740098, EBI-742688; CC P36406; G2XKQ0: SUMO1P1; NbExp=3; IntAct=EBI-740098, EBI-10175576; CC P36406; Q9BSH4: TACO1; NbExp=3; IntAct=EBI-740098, EBI-747797; CC P36406; Q13148: TARDBP; NbExp=3; IntAct=EBI-740098, EBI-372899; CC P36406; Q5VWN6-2: TASOR2; NbExp=3; IntAct=EBI-740098, EBI-10172380; CC P36406; Q9NU19: TBC1D22B; NbExp=8; IntAct=EBI-740098, EBI-8787464; CC P36406; Q15560: TCEA2; NbExp=3; IntAct=EBI-740098, EBI-710310; CC P36406; Q8N8B7-2: TCEANC; NbExp=3; IntAct=EBI-740098, EBI-11955057; CC P36406; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-740098, EBI-11139477; CC P36406; Q0P5Q0: TMSB4X; NbExp=3; IntAct=EBI-740098, EBI-10226570; CC P36406; P21580: TNFAIP3; NbExp=6; IntAct=EBI-740098, EBI-527670; CC P36406; Q13077: TRAF1; NbExp=3; IntAct=EBI-740098, EBI-359224; CC P36406; P36406: TRIM23; NbExp=7; IntAct=EBI-740098, EBI-740098; CC P36406; Q0P6H7: TRIM29; NbExp=3; IntAct=EBI-740098, EBI-10226710; CC P36406; Q14134: TRIM29; NbExp=4; IntAct=EBI-740098, EBI-702370; CC P36406; Q8IWZ5: TRIM42; NbExp=3; IntAct=EBI-740098, EBI-5235829; CC P36406; Q9BYV6: TRIM55; NbExp=2; IntAct=EBI-740098, EBI-2341179; CC P36406; Q12815: TROAP; NbExp=5; IntAct=EBI-740098, EBI-2349743; CC P36406; Q7Z6J9: TSEN54; NbExp=3; IntAct=EBI-740098, EBI-2559824; CC P36406; Q63HK5: TSHZ3; NbExp=3; IntAct=EBI-740098, EBI-9053916; CC P36406; Q86UY0: TXNDC5; NbExp=3; IntAct=EBI-740098, EBI-2825190; CC P36406; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-740098, EBI-10180829; CC P36406; Q9UMX0: UBQLN1; NbExp=6; IntAct=EBI-740098, EBI-741480; CC P36406; O75604: USP2; NbExp=3; IntAct=EBI-740098, EBI-743272; CC P36406; Q9Y2K6: USP20; NbExp=3; IntAct=EBI-740098, EBI-2511991; CC P36406; Q9BRU9: UTP23; NbExp=3; IntAct=EBI-740098, EBI-5457544; CC P36406; Q99990: VGLL1; NbExp=3; IntAct=EBI-740098, EBI-11983165; CC P36406; Q64LD2: WDR25; NbExp=3; IntAct=EBI-740098, EBI-744560; CC P36406; O76024: WFS1; NbExp=3; IntAct=EBI-740098, EBI-720609; CC P36406; B7ZLI8: WHR1; NbExp=3; IntAct=EBI-740098, EBI-10176124; CC P36406; Q05516: ZBTB16; NbExp=3; IntAct=EBI-740098, EBI-711925; CC P36406; Q9P1Z0: ZBTB4; NbExp=3; IntAct=EBI-740098, EBI-2564133; CC P36406; Q53FD0: ZC2HC1C; NbExp=3; IntAct=EBI-740098, EBI-740767; CC P36406; Q53FD0-2: ZC2HC1C; NbExp=3; IntAct=EBI-740098, EBI-14104088; CC P36406; Q8N6M9: ZFAND2A; NbExp=3; IntAct=EBI-740098, EBI-3921109; CC P36406; P17024: ZNF20; NbExp=3; IntAct=EBI-740098, EBI-717634; CC P36406; P15622-3: ZNF250; NbExp=3; IntAct=EBI-740098, EBI-10177272; CC P36406; Q9H9D4: ZNF408; NbExp=3; IntAct=EBI-740098, EBI-347633; CC P36406; Q8TAU3: ZNF417; NbExp=3; IntAct=EBI-740098, EBI-740727; CC P36406; Q6S9Z5: ZNF474; NbExp=3; IntAct=EBI-740098, EBI-17269964; CC P36406; Q8TBZ8: ZNF564; NbExp=6; IntAct=EBI-740098, EBI-10273713; CC P36406; Q9P0T4: ZNF581; NbExp=8; IntAct=EBI-740098, EBI-745520; CC P36406; Q96SQ5: ZNF587; NbExp=3; IntAct=EBI-740098, EBI-6427977; CC P36406; A0A0S2Z5X4: ZNF688; NbExp=3; IntAct=EBI-740098, EBI-16429014; CC P36406; A0A0S2Z6P0: ZNF688; NbExp=3; IntAct=EBI-740098, EBI-16429989; CC P36406; Q9Y2P0: ZNF835; NbExp=3; IntAct=EBI-740098, EBI-5667516; CC P36406; P09022: Hoxa1; Xeno; NbExp=2; IntAct=EBI-740098, EBI-3957603; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28871090, CC ECO:0000269|PubMed:38769438}. Endomembrane system CC {ECO:0000269|PubMed:9671726}. Golgi apparatus membrane CC {ECO:0000269|PubMed:9671726}. Lysosome membrane CC {ECO:0000269|PubMed:9671726}. Cytoplasm, P-body CC {ECO:0000269|PubMed:38769438}. Note=Membrane-associated with the Golgi CC complex and lysosomal structures. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=Alpha; CC IsoId=P36406-1; Sequence=Displayed; CC Name=Beta; CC IsoId=P36406-2; Sequence=VSP_000296; CC Name=Gamma; CC IsoId=P36406-3; Sequence=VSP_000297; CC -!- DOMAIN: The RING-type zinc finger domain is responsible for E3 CC ubiquitin ligase activity. This domain is catalytically active as a CC dimer. {ECO:0000269|PubMed:28681414}. CC -!- PTM: Phosphorylation at Ser-39 triggers TRIM23 autoubiquitination and CC GTPase activity. {ECO:0000269|PubMed:40360474}. CC -!- PTM: Auto-ubiquitinated. {ECO:0000269|PubMed:40360474}. CC -!- SIMILARITY: In the C-terminal section; belongs to the small GTPase CC superfamily. Arf family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; L04510; AAA35940.1; -; mRNA. DR EMBL; AF230397; AAG50176.1; -; mRNA. DR EMBL; AF230398; AAG50177.1; -; mRNA. DR EMBL; AF230399; AAG50178.1; -; mRNA. DR EMBL; BC022510; AAH22510.1; -; mRNA. DR CCDS; CCDS3986.1; -. [P36406-3] DR CCDS; CCDS3987.1; -. [P36406-1] DR CCDS; CCDS43322.1; -. [P36406-2] DR PIR; A46054; A46054. DR RefSeq; NP_001647.1; NM_001656.4. [P36406-1] DR RefSeq; NP_150230.1; NM_033227.3. [P36406-2] DR RefSeq; NP_150231.1; NM_033228.3. [P36406-3] DR RefSeq; XP_016864933.1; XM_017009444.3. [P36406-2] DR RefSeq; XP_054208503.1; XM_054352528.1. [P36406-1] DR RefSeq; XP_054208504.1; XM_054352529.1. [P36406-1] DR RefSeq; XP_054208505.1; XM_054352530.1. [P36406-1] DR RefSeq; XP_054208507.1; XM_054352532.1. [P36406-2] DR PDB; 5VZV; X-ray; 1.81 A; A/B/C=1-123. DR PDB; 5VZW; X-ray; 2.28 A; F/G=1-123. DR AlphaFoldDB; P36406; -. DR SMR; P36406; -. DR BioGRID; 106868; 385. DR FunCoup; P36406; 1193. DR IntAct; P36406; 241. DR MINT; P36406; -. DR NDEx; IQUERY-CP-TRIM23; 2 NDEx IQuery Curated Pathways. DR STRING; 9606.ENSP00000231524; -. DR iPTMnet; P36406; -. DR PhosphoSitePlus; P36406; -. DR BioMuta; TRIM23; -. DR DMDM; 543839; -. DR jPOST; P36406; -. DR MassIVE; P36406; -. DR PaxDb; 9606-ENSP00000231524; -. DR PeptideAtlas; P36406; -. DR ProteomicsDB; 55200; -. [P36406-1] DR ProteomicsDB; 55201; -. [P36406-2] DR ProteomicsDB; 55202; -. [P36406-3] DR Pumba; P36406; -. DR Antibodypedia; 11584; 265 antibodies from 35 providers. DR DNASU; 373; -. DR Ensembl; ENST00000231524.14; ENSP00000231524.9; ENSG00000113595.15. [P36406-1] DR Ensembl; ENST00000274327.11; ENSP00000274327.7; ENSG00000113595.15. [P36406-3] DR Ensembl; ENST00000381018.7; ENSP00000370406.3; ENSG00000113595.15. [P36406-2] DR GeneID; 373; -. DR KEGG; hsa:373; -. DR MANE-Select; ENST00000231524.14; ENSP00000231524.9; NM_001656.4; NP_001647.1. DR UCSC; uc003jtw.4; human. [P36406-1] DR AGR; HGNC:660; -. DR ClinPGx; PA24943; -. DR CTD; 373; -. DR DisGeNET; 373; -. DR GeneCards; TRIM23; -. DR HGNC; HGNC:660; TRIM23. DR HPA; ENSG00000113595; Low tissue specificity. DR MIM; 601747; gene. DR OpenTargets; ENSG00000113595; -. DR VEuPathDB; HostDB:ENSG00000113595; -. DR eggNOG; KOG0070; Eukaryota. DR eggNOG; KOG4185; Eukaryota. DR GeneTree; ENSGT00940000158562; -. DR HOGENOM; CLU_033905_0_0_1; -. DR InParanoid; P36406; -. DR OMA; IQACDAK; -. DR OrthoDB; 2011769at2759; -. DR PAN-GO; P36406; 6 GO annotations based on evolutionary models. DR PhylomeDB; P36406; -. DR BRENDA; 2.3.2.27; 2681. DR PathwayCommons; P36406; -. DR SignaLink; P36406; -. DR SIGNOR; P36406; -. DR UniPathway; UPA00143; -. DR Agora; ENSG00000113595; -. DR BioGRID-ORCS; 373; 16 hits in 1199 CRISPR screens. DR GeneWiki; TRIM23; -. DR GenomeRNAi; 373; -. DR Pharos; P36406; Tbio. DR PRO; PR:P36406; -. DR Proteomes; UP000005640; Chromosome 5. DR RNAct; P36406; protein. DR Bgee; ENSG00000113595; Expressed in cerebellar vermis and 189 other cell types or tissues. DR ExpressionAtlas; P36406; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProt. DR GO; GO:0000139; C:Golgi membrane; IDA:HGNC-UCL. DR GO; GO:0005765; C:lysosomal membrane; IDA:HGNC-UCL. DR GO; GO:0005634; C:nucleus; IEA:Ensembl. DR GO; GO:0000932; C:P-body; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0008047; F:enzyme activator activity; TAS:ProtInc. DR GO; GO:0019003; F:GDP binding; IDA:HGNC-UCL. DR GO; GO:0005525; F:GTP binding; IDA:HGNC-UCL. DR GO; GO:0003924; F:GTPase activity; IDA:HGNC-UCL. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0061630; F:ubiquitin protein ligase activity; IDA:UniProtKB. DR GO; GO:0004842; F:ubiquitin-protein transferase activity; IDA:HGNC-UCL. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006886; P:intracellular protein transport; IBA:GO_Central. DR GO; GO:0010508; P:positive regulation of autophagy; IDA:UniProt. DR GO; GO:0016567; P:protein ubiquitination; IDA:HGNC-UCL. DR CDD; cd04158; ARD1; 1. DR CDD; cd19773; Bbox2_TRIM23_C-IX_rpt1; 1. DR CDD; cd19774; Bbox2_TRIM23_C-IX_rpt2; 1. DR CDD; cd16645; mRING-HC-C3HC3D_TRIM23_C-IX; 1. DR FunFam; 3.30.160.60:FF:000440; E3 ubiquitin-protein ligase TRIM23; 1. DR FunFam; 3.30.40.10:FF:000130; E3 ubiquitin-protein ligase TRIM23; 1. DR FunFam; 3.40.50.300:FF:000486; E3 ubiquitin-protein ligase TRIM23; 1. DR Gene3D; 3.30.160.60; Classic Zinc Finger; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR Gene3D; 3.30.40.10; Zinc/RING finger domain, C3HC4 (zinc finger); 1. DR InterPro; IPR003649; Bbox_C. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd. DR InterPro; IPR024156; Small_GTPase_ARF. DR InterPro; IPR006689; Small_GTPase_ARF/SAR. DR InterPro; IPR027370; Znf-RING_euk. DR InterPro; IPR000315; Znf_B-box. DR InterPro; IPR013087; Znf_C2H2_type. DR InterPro; IPR001841; Znf_RING. DR InterPro; IPR013083; Znf_RING/FYVE/PHD. DR InterPro; IPR017907; Znf_RING_CS. DR NCBIfam; TIGR00231; small_GTP; 1. DR PANTHER; PTHR11711; ADP RIBOSYLATION FACTOR-RELATED; 1. DR Pfam; PF00025; Arf; 1. DR Pfam; PF00643; zf-B_box; 1. DR Pfam; PF13445; zf-RING_UBOX; 1. DR PRINTS; PR00328; SAR1GTPBP. DR SMART; SM00177; ARF; 1. DR SMART; SM00502; BBC; 1. DR SMART; SM00336; BBOX; 2. DR SMART; SM00175; RAB; 1. DR SMART; SM00184; RING; 1. DR SMART; SM00178; SAR; 1. DR SUPFAM; SSF57845; B-box zinc-binding domain; 1. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR SUPFAM; SSF57850; RING/U-box; 1. DR PROSITE; PS51417; ARF; 1. DR PROSITE; PS50119; ZF_BBOX; 1. DR PROSITE; PS00518; ZF_RING_1; 1. DR PROSITE; PS50089; ZF_RING_2; 1. DR PDBsum; 5VZV; -. DR PDBsum; 5VZW; -. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Coiled coil; Cytoplasm; KW Golgi apparatus; GTP-binding; Host-virus interaction; Immunity; KW Innate immunity; Lysosome; Membrane; Metal-binding; Nucleotide-binding; KW Phosphoprotein; Proteomics identification; Reference proteome; Transferase; KW Ubl conjugation; Ubl conjugation pathway; Zinc; Zinc-finger. FT CHAIN 1..574 FT /note="E3 ubiquitin-protein ligase TRIM23" FT /id="PRO_0000207483" FT ZN_FING 31..76 FT /note="RING-type; degenerate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00175" FT ZN_FING 122..168 FT /note="B box-type; degenerate" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00024" FT REGION 390..574 FT /note="ARF-like" FT COILED 352..379 FT /evidence="ECO:0000255" FT BINDING 411..418 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 454..458 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT BINDING 513..516 FT /ligand="GTP" FT /ligand_id="ChEBI:CHEBI:37565" FT /evidence="ECO:0000250" FT MOD_RES 39 FT /note="Phosphoserine" FT /evidence="ECO:0000269|PubMed:40360474" FT VAR_SEQ 541..574 FT /note="WYIQGCDARSGMGLYEGLDWLSRQLVAAGVLDVA -> CFSDNM (in FT isoform Gamma)" FT /evidence="ECO:0000303|PubMed:11331580" FT /id="VSP_000297" FT VAR_SEQ 551..574 FT /note="GMGLYEGLDWLSRQLVAAGVLDVA -> VFQIICDQYTGKEVVTEKG (in FT isoform Beta)" FT /evidence="ECO:0000303|PubMed:11331580" FT /id="VSP_000296" FT VARIANT 480 FT /note="D -> N (in dbSNP:rs34046496)" FT /id="VAR_048320" FT MUTAGEN 34 FT /note="C->A: Loss of E3 ubiquitin-protein ligase activity." FT /evidence="ECO:0000269|PubMed:15684077" FT MUTAGEN 39 FT /note="S->A: Exhibits a near-complete loss of FT 'Lys-27'-linked ubiquitination." FT /evidence="ECO:0000269|PubMed:40360474" FT MUTAGEN 39 FT /note="S->D: No loss of 'Lys-27'-linked ubiquitination." FT /evidence="ECO:0000269|PubMed:40360474" FT MUTAGEN 53 FT /note="H->A: Loss of E3 ubiquitin-protein ligase activity." FT /evidence="ECO:0000269|PubMed:15684077" FT MUTAGEN 418 FT /note="T->N: Maintains GTPase activity. Increases FT interaction with PSCD1." FT /evidence="ECO:0000269|PubMed:10748148" FT MUTAGEN 458 FT /note="K->I: Suppresses GTPase activity. Decreases FT interaction with PSCD1." FT /evidence="ECO:0000269|PubMed:10748148" FT TURN 32..34 FT /evidence="ECO:0007829|PDB:5VZV" FT STRAND 40..42 FT /evidence="ECO:0007829|PDB:5VZV" FT STRAND 46..48 FT /evidence="ECO:0007829|PDB:5VZV" FT STRAND 54..56 FT /evidence="ECO:0007829|PDB:5VZV" FT HELIX 57..62 FT /evidence="ECO:0007829|PDB:5VZV" FT STRAND 69..71 FT /evidence="ECO:0007829|PDB:5VZV" FT TURN 73..75 FT /evidence="ECO:0007829|PDB:5VZV" FT STRAND 78..80 FT /evidence="ECO:0007829|PDB:5VZV" FT HELIX 85..88 FT /evidence="ECO:0007829|PDB:5VZV" FT HELIX 93..103 FT /evidence="ECO:0007829|PDB:5VZV" SQ SEQUENCE 574 AA; 64067 MW; CB85923B29BF0320 CRC64; MATLVVNKLG AGVDSGRQGS RGTAVVKVLE CGVCEDVFSL QGDKVPRLLL CGHTVCHDCL TRLPLHGRAI RCPFDRQVTD LGDSGVWGLK KNFALLELLE RLQNGPIGQY GAAEESIGIS GESIIRCDED EAHLASVYCT VCATHLCSEC SQVTHSTKTL AKHRRVPLAD KPHEKTMCSQ HQVHAIEFVC LEEGCQTSPL MCCVCKEYGK HQGHKHSVLE PEANQIRASI LDMAHCIRTF TEEISDYSRK LVGIVQHIEG GEQIVEDGIG MAHTEHVPGT AENARSCIRA YFYDLHETLC RQEEMALSVV DAHVREKLIW LRQQQEDMTI LLSEVSAACL HCEKTLQQDD CRVVLAKQEI TRLLETLQKQ QQQFTEVADH IQLDASIPVT FTKDNRVHIG PKMEIRVVTL GLDGAGKTTI LFKLKQDEFM QPIPTIGFNV ETVEYKNLKF TIWDVGGKHK LRPLWKHYYL NTQAVVFVVD SSHRDRISEA HSELAKLLTE KELRDALLLI FANKQDVAGA LSVEEITELL SLHKLCCGRS WYIQGCDARS GMGLYEGLDW LSRQLVAAGV LDVA //